Matrix metalloproteinases: Master regulators of tissue morphogenesis

The matrix metalloproteinases (MMPs) are a class of zinc proteases that aid in breaking most of the extracellular matrix's (ECM) constituents. Additionally, MMPs play a part in processing elements that affect inflammation, cell development and proliferation, and many more. In vivo genetic study of the Drosophila MMPs Mmp1 and Mmp2 reveals they are essential for tissue remodeling but not embryonic development. The canonical and conserved MMP domain organization is present in both fly MMPs. Because Mmp2 appeared to be membrane-anchored and Mmp1 appeared to be released, the pericellular localization of Drosophila MMPs has been used to classify them. This suggests that the protein's localization is the critical distinction in this small MMP family. The signal sequence, the propeptide, the catalytic domain, and the hemopexin-like domain are among the numerous domains found in MMPs. Following secretion from the extracellular environment to the endoplasmic reticulum, the pre-domain, also known as the signal sequence, serves to direct MMP production. MMPs of the secretory and membrane types (MT-MMPs) are two groups of MMPs that have been widely recognized. Subgroups of MMPs are categorized based on their structure and function. While analysis of the intracellular activity of human MMPs is challenging because the human genome contains around 23 distinct MMPs with overlapping functions, only two MMPs, dMMP1 and dMMP2, are encoded by the Drosophila melanogaster genome. On the other hand, the balance between MMPs and the family members are implicated in various pathophysiology/progression of diseases, but whether or not the mechanisms of MMP inhibition are not clearly understood as master regulators. In this review, we outline the role of MMPs as master regulators of tissue morphogenesis.